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Database: UniProt
Entry: D8PMP5_SCHCM
LinkDB: D8PMP5_SCHCM
Original site: D8PMP5_SCHCM 
ID   D8PMP5_SCHCM            Unreviewed;      1450 AA.
AC   D8PMP5;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Lysophospholipase NTE1 {ECO:0000256|ARBA:ARBA00018317, ECO:0000256|RuleBase:RU362043};
DE            EC=3.1.1.5 {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362043};
DE   AltName: Full=Intracellular phospholipase B {ECO:0000256|RuleBase:RU362043};
GN   ORFNames=SCHCODRAFT_72754 {ECO:0000313|EMBL:EFJ02164.1};
OS   Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX   NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN   [1] {ECO:0000313|EMBL:EFJ02164.1, ECO:0000313|Proteomes:UP000007431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX   PubMed=20622885; DOI=10.1038/nbt.1643;
RA   Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA   de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA   Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA   Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA   Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA   Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA   Woesten H.A.B.;
RT   "Genome sequence of the model mushroom Schizophyllum commune.";
RL   Nat. Biotechnol. 28:957-963(2010).
CC   -!- FUNCTION: Intracellular phospholipase B that catalyzes the double
CC       deacylation of phosphatidylcholine (PC) to glycerophosphocholine
CC       (GroPCho). Plays an important role in membrane lipid homeostasis.
CC       {ECO:0000256|RuleBase:RU362043}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC         Evidence={ECO:0000256|RuleBase:RU362043};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU362043}.
CC   -!- SIMILARITY: Belongs to the NTE family. {ECO:0000256|ARBA:ARBA00006636,
CC       ECO:0000256|RuleBase:RU362043}.
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DR   EMBL; GL377302; EFJ02164.1; -; Genomic_DNA.
DR   RefSeq; XP_003037066.1; XM_003037020.1.
DR   STRING; 578458.D8PMP5; -.
DR   GeneID; 9597510; -.
DR   KEGG; scm:SCHCO_02530966; -.
DR   VEuPathDB; FungiDB:SCHCODRAFT_02530966; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   HOGENOM; CLU_000960_1_1_1; -.
DR   InParanoid; D8PMP5; -.
DR   OMA; SSGYVWR; -.
DR   OrthoDB; 5303733at2759; -.
DR   Proteomes; UP000007431; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR   CDD; cd00038; CAP_ED; 2.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 3.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR001423; LysoPLipase_patatin_CS.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR14226:SF29; NEUROPATHY TARGET ESTERASE SWS; 1.
DR   PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00100; cNMP; 2.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 3.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS51635; PNPLA; 1.
DR   PROSITE; PS01237; UPF0028; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU362043};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01161};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW   ProRule:PRU01161};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|PROSITE-
KW   ProRule:PRU01161}; Membrane {ECO:0000256|RuleBase:RU362043};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007431};
KW   Transmembrane {ECO:0000256|RuleBase:RU362043};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362043}.
FT   TRANSMEM        27..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362043"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362043"
FT   DOMAIN          652..760
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          773..893
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          1144..1308
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   REGION          278..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1425..1450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1148..1153
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   MOTIF           1175..1179
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   MOTIF           1295..1297
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        283..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..520
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1430..1445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1177
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1295
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   1450 AA;  159537 MW;  6E07A9BAE99CDF9E CRC64;
     MSELSPDVSA SATAAAADVS SHPLVSLISA CFWVILWALS WVKSLIGIVT ISVPRLVYQI
     LSYSMTLTLN FWSFVLIFGT CAVALNYFIR FRYLNDYMQL KEPPLGKPDV KELHPDVNTA
     DEPANFHNYL DDFLQAVRVF GFLEKPVFHE LARHLQTRRL IAGDSISLDQ DRSFYCVVDG
     TVQVFAKSDD EHTASGSGQW DDEDINGYHL MNEVTSGGTV SSLFTILSLF TEDVKISWQD
     ADESPKRTHR SRKSTDERIR VNSDVSYFNL ERPALVRTPL SNPGLRRRSS TSSSASTVQP
     EESPTTPEDL RRTASPPPLS ERSYAPSTPV HHIQGPVQIH RGVVARATED TTLAVIPAEA
     FRRLTKKFPK ATGHIVQVIL TRFARVTFNA AHKYLGLTSE VLRAEKSIND LACHPLPPSF
     YEGGGLQQLR HRFEVPPSGS DSDNDYFTHT GARTHSPNPM STYSPNPMSA QESSTDSDDS
     HPAFIRTASS STARPGSRSS TISSPNLTKT SGSRMNVQAG DLLSSTANTS RLLRPINRTA
     MTPRVPLRAV VEHQSPERAL GEEFNLREEV MSCIAKSIGL LQPPISGNDS LEGSPKLNPF
     ERSRSPMPSS FGSLSLLDLG DDASSTMTGG SASIQSGSGM SGLDNEVEIL FFPAGATLTK
     AGDISTGLYY VIEGFLDILL PLEKEKQRAS DRPGAKNPGK GPNKKPHDDS ETHKFLFTVK
     PGGIAGYLAS LSNTASYVDI VAKTDTYVGY LPAQALERLL EKRPIVLLTL AKRLISLLSP
     LVLQIDASLD WMQVNAGQII WRPEDASDCF YIVINGRLRA ITETEKGDVS IVGEYGQGDA
     VGELDVITSS PRQNTLHAIR DTELIRMPQT LFNALSMRDP RTTQQILRKI ALRVRDEAEG
     GKTSQSRPPM EVKSSNANLK TICILPVSRA VPIDVFARKL QTALEGIGAS TVYLNQASVA
     NRLGRHVFTR MGKLKAAGWL ADQEQRYRTV LYVADSPVNN SWTQTCIRQA DCVMVVGMGD
     DASIGEYERL LLSTKTTAKK ELVLLHPDRS VAPGSTREWL KNRPWIHQHI HVELPGLVIP
     ITKSTAHLPK DPDPIIALKN FKDKVQSELK KYRGTVGDAR PQRLPHVNDF SRLARRICGK
     SIGLVLGGGG ARGVSHLGLI RALEEYGIPV DHVGGTSIGA FIGGLYAREG DSLSSAGRAK
     QFSGRMGNIW RMLSDVTYPI VAYTTGHEFN RAIYKSFYDL HIEDMWLPFF CNTTNITTSG
     MDIHETGYAW RFIRGSMTLV GLLPPLCDNG NMHVDGGYVD NLPVSTMFSM GSSAVFACDV
     GSIDDNSPRN FGDSVSGWWL FINRWNPFSD ASRVPAITEI QSRLAYVSSV RTLEEAKVAP
     GCLYIAMPVQ EYGTLQFSKF EELQKIGYEA GMKALAKWDE EGRLPSPFID GKQQFSSSKK
     QGRAARRNSI
//
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